Preparation and characterization of bovine aortic actin
| Autor: | C Axelrud-Cavadore, Jean-Claude Cavadore, Philippe Berta, J Haiech, M C Harricane |
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| Jazyk: | angličtina |
| Rok vydání: | 1985 |
| Předmět: |
Macromolecular Substances
ATPase macromolecular substances Biochemistry Muscle Smooth Vascular Myosin Endopeptidases Animals Actin-binding protein Amino Acids Phosphorylation Protein kinase A Molecular Biology Actin Aorta chemistry.chemical_classification Adenosine Triphosphatases biology Kinase Cell Biology Actins Peptide Fragments Amino acid Enzyme Activation Microscopy Electron chemistry biology.protein Cattle Electrophoresis Polyacrylamide Gel MDia1 Ca(2+) Mg(2+)-ATPase Research Article |
| Popis: | A functional vascular smooth-muscle actin from bovine aorta was purified to homogeneity by an original method and was able to polymerize. Aortic actin is composed of two major isoforms and at least two minor ones. This actin was not phosphorylated by either cyclic AMP-dependent protein kinase or C kinase. The physical properties of aortic actin were found to be very similar to those of skeletal-muscle actin, except for amino acid composition (three tryptophan residues instead of four). The aortic actin and skeletal-muscle actin differ in the extent of activation of the Mg-dependent ATPase of skeletal-muscle myosin. |
| Databáze: | OpenAIRE |
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